Related Experiment Video
Updated: May 25, 2026

Preparation of Oligomeric β-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices
Published on: July 14, 2010
Binding of β-amyloid to sulfated sugar residues in a polymer brush
Hiromi Kitano1, Daisuke Saito, Tomohiro Kamada
1Department of Applied Chemistry, Graduate School of Science and Engineering, University of Toyama, Toyama, Japan. kitano@eng.u-toyama.ac.jp
Abstract:
A glycopolymer obtained by living radical polymerization of glucose-carrying vinyl monomer was sulfated and accumulated as a polymer brush on a gold colloid-immobilized glass. Binding processes of various proteins to sulfated glucose residues in the brush were examined by the increase in absorbance with a help of localized surface plasmon resonance. β-Amyloid protein (Aβ) bound to the sulfated glycopolymer brush, whereas no binding to the non-sulfated one. An AFM image of Aβ aggregates on the sulfated brush was ellipsoidal, whereas no-shaped aggregation of Aβ on the poly(methacrylic acid) and poly[2-(dimethylamino)ethyl methacrylate] brushes. The present results indicate the importance of balance between electrostatic attraction and repulsion in the folding-aggregation phenomena of Aβ at the surface of glycopolymers.
Related Concept Videos
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Oligosaccharide Assembly
Multiple sugar molecules that may or may...
Alzheimer Disease ll: Pathophysiology
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme can...
Protein Glycosylation
Glycosylation occurs in...

